4

4. El equilibrio conformacional de las proteínas. Estrategias y ejemplos de estabilización mediante interacciones electrostáticas y puentes de hidrógeno, interacciones hidrófobas y fuerzas de van der Waals. Estabilizaciones de tipo entrópico.

Bibliografía:

Proteins. Structures and molecular properties, 2nd ed. T.E. Creighton. Freeman and Company, New York, 1993.

Introduction to protein structure. C. Branden & J. Tooze. 1999. Garland Publishing, Inc. New York.

Physical basis of the folded conformation of proteins. Privalov, P.L.(1992) in Protein folding (Creighton, T.E. Ed. ) pp 83-126, W.H. Freeman, New York.

Protein structure and the energetics of protein stability. A. D. Robertson, & K.P. Murphy (1997) Chem. REv. 97, 1251-1267

Engineering enzymes for stability. A. Shaw & R. Bott. COSB 6 546-550 (1996)

Principles of protein stability derived from protein engineering experiments. A.R. Fersht & L. Serrano. COSB 3, 75-83 (1993)

Measuring the conformational stability of a protein. Pace, C.N., Shirley, B.A. & Thomson, J.A. (1989) in Protein structure. A practical approach (Creighton, T.E. Ed.) pp 311-330, IRL Press, Oxford.

The folding of an enzyme II: substructure of barnase and the contribution of different interactions to protein stability. Serrano, L., Kellis, J.T. Jr., Cann, P., Matouschek, A & Fersht, A.R. (1992) J. Mol. Biol. 224, 783-804.

Long-range charge-charge interactions in proteins. Comparison of experimental resulta with calculations from a theoretical method. R. Loewenthal, J. Sancho, T. Reinikainen, & A. R. Fersht. J. Mol. Biol.. 232, 574-583 (1993).

Surface electrostatic interactions contribute little to stability of barnase. Sali, D., Bycroft, M., & Fersht, A.R. (1988) J. Mol. Biol. 220, 779-788.

The hydrogen bond in molecular recognition. Fersht, A.R. (1987) Trends Biol. Sci 12, 301-304.

Hydrogen bonding stabilises globular proteins. J.K. Myers, & C.N. Pace (1996) Biophys. J. 71, 2033-2039

Histidine-aromatic interactions in barnase. elevation of histidine pKa and contribution to protein stability. Loewenthal, R., Sancho, J. & Fersht, A.R. (1992). J. Mol. Biol. 224, 759-770.

Cation-p interactions in chemistry and biology: a new view of benzene, Phe, Tyr and Trp. Dougherty, D.A. (1996) . Science, 271, 163-168.

The cation-p interaction. Ma, J.A. (1997) . Chem. Rev. 97, 1303-1324.A. (1997) . Chem. Rev. 97, 1303-1324;

Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Burley, S.K. & Petsko, G.A. Science 229, 23-28 (1985)

Enhanced protein thermostability from designed mutations that interact with a-helix dipoles. Nicholson, H, Becktel, W.J. & Matthews, B.W.(1988). Nature 336, 651-656 (1988)

Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. M. Karpusas, Baase, W.A., Matsumara, M. & Matthews, B.W. Proc. Nat. Acad. Sci. 86, 8237-41 (1989)

A cavity containing mutant of T4 lysozyme is stabilized by buried benzene. Eriksson, A.E., Baase, W.A., Wozniak, J.A., Matthews, B.W. Nature 355, 371-373 (1992).

Reverse hydrophobic effects relieved by amino acid substitutions at a protein surface. Pakula, A.A. & Sauer, R.T. (1990) Nature 344, 363-364

Substantial increase of protein stability by multiple disulfide bonds. Matsumara, M., Signor, G. Matthews & B.W. Nature 342:291 (1989).

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Matthews, B.W, Nicholson, H & Becktel, W.J. Proc. Nat. Acad. Sci. 71, 4178-82 (1987)

Capping and a-helix stability. L. Serrano & A.R. Fersht. Nature 342, 296-299 (1989)

Design and structural analysis of an engineered thermostable chicken lysozyme. Shih, P. & Kirsch, J.K. (1995) Prot. Sci. 4:2062-2072

Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. Zhang, X-J, Baase, W.A., Shoichet, B.K., Wilson, K.P.,& Matthews, B.K. Prot. Eng. 8: 1017-1022

Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. V.V. Loladze, B. Ibarra-Molero, J.M. Sánchez-Ruiz & G.I. Makhatadze. Biochemistry 38, 16419-16423.